Abstract

Channels regulated by cyclic nucleotides are key signalling proteins in several biological pathways. The regulatory aspect is conferred by a C-terminal cyclic nucleotide-binding domain (CNBD). We report resonance assignments of the CNBD of a bacterial mlCNG channel obtained using 2D and 3D solid-state NMR under Magic-angle Spinning conditions. A secondary chemical shift analysis of the 141 residue protein suggests a three-dimensional fold seen in earlier X-ray and solution-state NMR work and points to spectroscopic polymorphism for a selected set of resonances.Electronic supplementary materialThe online version of this article (doi:10.1007/s12104-012-9363-4) contains supplementary material, which is available to authorized users.

Highlights

  • Channels regulated by cyclic nucleotides are key signalling proteins in several biological pathways

  • We report resonance assignments of the cyclic nucleotide-binding domain (CNBD) of a bacterial mlCNG channel obtained using 2D and 3D solid-state NMR under Magicangle Spinning conditions

  • A secondary chemical shift analysis of the 141 residue protein suggests a threedimensional fold seen in earlier X-ray and solution-state NMR work and points to spectroscopic polymorphism for a selected set of resonances

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Summary

Biological context

Cyclic nucleotides (cNMPs) are important secondary messenger molecules that mediate a multitude of processes by activating several different proteins in the signalling cascade. These proteins share a conserved regulatory protein unit referred to as cyclic nucleotide-binding domain. Upon binding cNMPs the regulatory CNBD renders the protein in an active conformation. The bacterial mlCNG channel displays distinctively different channel functioning property in being non-cooperative (Cukkemane et al 2007; Nimigean et al 2004). This provides a facile system in understanding the binding–gating relationship. We investigated the CNBD of mlCNG channel using solid-phase preparations paving the way for structural studies on the full-length channel

Methods and experiments
Assignments and data deposition
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